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A3CVP2 (SYA_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:Memar_1513
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

Protein attributes

Sequence length915 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036_A

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 915915Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074512

Sites

Metal binding6091Zinc By similarity
Metal binding6131Zinc By similarity
Metal binding7121Zinc By similarity
Metal binding7161Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CVP2 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: B9F5C81F183BA4FE

FASTA915101,646
        10         20         30         40         50         60 
MLEEEYTLDY FRSEGFERKV CKSCGAAFWT RDPEQEFCGD APCVTYNFIG NPVFKPHNVS 

        70         80         90        100        110        120 
EMREAFLSFF ERHGHTRLER YPVAARWRDD IYLTIASIAD FQPFVTSGVV PPPANPLTIS 

       130        140        150        160        170        180 
QPCIRLNDLD SVGRSGRHLT LFEMMAHHAF NTPEEQIYWK DQTVALCDEF IKSIGGDPAR 

       190        200        210        220        230        240 
VSYKEHPWYG GGNAGASVEV LIGGLEVATL VFMNLGRQKT DQPPVDVNGV PYYPMRLNIV 

       250        260        270        280        290        300 
DTGYGLERLV WASKGSPTIY DAVFPEMVSR LMRSARLEDL LDNPEFTKIM GLSARFAGVM 

       310        320        330        340        350        360 
DISGTNLYNL RRKVAEAIDV PVERLERIVV PIEKVYSIAD HTRCLAYMLG DCIVPSNVRE 

       370        380        390        400        410        420 
GYLARLVLRR TLRMMNDLSM DDALTDLIEA QMQVVGAENF EQDVDAVREI VENEEARYAS 

       430        440        450        460        470        480 
TLERGARIVQ KIARNYRAKS SRVPLEEVIT LYDSHGIPPE MVKEVAAAEG AVVEIPDNFY 

       490        500        510        520        530        540 
SLIAETHSEA QKEARGEDPL DAYRERAVSL PPTKKLYYEL PNEVEFEAMV LDYFDGMAVL 

       550        560        570        580        590        600 
DQTLFYPEGG GQPSDTGTLV TSESMVRVEE VVKLGEVILH RVTGGPLMRG DRVKGMVDEE 

       610        620        630        640        650        660 
RRWSLMRHHT ATHVLLHAAQ QVLGVHVHQA GAQKGSEVSR LDIRHYRHIT PDELRRIELE 

       670        680        690        700        710        720 
ANRLVMADTP VYIHVEERTK AEQKYGFGLY QGGVPPGREI RTVQVGADVQ ACAGTHVRTT 

       730        740        750        760        770        780 
GEIGPIRVLG VEHIQDGVER LVFAAGIAAV HAVQHLGDLL QESADMVSVQ PENLPATVAR 

       790        800        810        820        830        840 
FFSEWKEQKK EIERLQKKVV DLEMQNLDGE VVDGVRVVVR TLDATHKELV ALATTVADEG 

       850        860        870        880        890        900 
GVALFASSDG TVKVVATSGA PTVNAVDIVR EVCGILGGKG GGKPNLAQGA GPDASRLEEA 

       910 
LEYGRNRIIE ALHGE 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed: 21304656] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN57442.1.
RefSeqYP_001047424.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CVP2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3CVP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4846756.
GenomeReviewsGene locus Memar_1513 in contig CP000562_GR.
KEGGmem:Memar_1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAEIDIFRT.
PhylomeDBA3CVP2.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMMAR368407:MEMAR_1513-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_synth_arc.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_METMJ
AccessionPrimary (citable) accession number: A3CVP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 20, 2007
Last modified: January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families